Complex of simian virus 40 large tumor antigen and 48,000-dalton host tumor antigen.
Complex of simian virus 40 large tumor antigen and 48,000-dalton host tumor antigen.
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猿猴病毒 40 大肿瘤抗原和 48,000 道尔顿宿主肿瘤抗原的复合物。
DOI：
10.1073/pnas.78.1.105
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发表时间：
1981
影响因子：
11.1
通讯作者：
Carroll,RB
中科院分区：
文献类型：
--
作者：
Greenspan,DS;Carroll,RB
用蔗糖梯度沉淀法可将猴病毒40大分子肿瘤抗原(T-Ag)分离为快速沉淀、磷酸化程度最高的部分和缓慢沉淀、磷酸化程度较低的部分。MR 48,000宿主肿瘤抗原(48,000 HTA，也称为非病毒T抗原)优先与最大程度磷酸化的T抗原络合。脉冲标记的T-Ag以5-6S单体的形式沉积，而放射性标记的T-Ag的时间逐渐延长，沉降系数缓慢增加，给出了5-S和大于28 S的广泛分布。病毒A基因的突变导致T-Ag的磷酸化减少，48,000个HTA结合显著减少，使T-Ag的沉降系数向单体值移动。磷酸化程度越高的T-Ag对染色质的亲和力也越高。
Simian virus 40 large tumor antigen (T Ag) can be separated by sucrose gradient sedimentation into a rapidly sedimenting, maximally phosphorylated fraction and a slowly sedimenting, less phosphorylated fraction. The Mr 48,000 host tumor antigen (48,000 HTA, also called nonviral T Ag) is preferentially complexed with the maximally phosphorylated T Ag. Pulse-labeled T Ag sediments as a 5-6S monomer, whereas T Ag radiolabeled for progressively longer periods slowly increases in sedimentation coefficient to give a broad distribution between 5 S and greater than 28 S. Mutation in the viral A locus causes a decrease in T Ag phosphorylation and a marked decrease in 48,000 HTA binding, shifting the sedimentation coefficient of T Ag to the monomer value. The more highly phosphorylated T Ag also has the highest affinity for chromatin.